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Dihydroneopterin aldolase is an enzyme involved in the folate biosynthetic pathway, catalyzing the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. It is a promising target for developing antimicrobial drugs due to its absence in mammals, which makes it a selective target for disrupting bacterial metabolism without affecting human cells. The enzyme does not require metal ions or Schiff base formation for catalysis, making it unique among aldolases.
Inhibition of DHNA activity disrupts folate biosynthesis in bacteria, inhibiting bacterial growth.
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